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Full text data of YKT6

YKT6 [Confidence: low (only semi-automatic identification from reviews)]
Synaptobrevin homolog YKT6; 2.3.1.-; Flags: Precursor

UniProt O15498
ID YKT6_HUMAN Reviewed; 198 AA.
AC O15498; Q53F01; Q6FGU9; Q6IB15;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Synaptobrevin homolog YKT6;
DE EC=2.3.1.-;
DE Flags: Precursor;
GN Name=YKT6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Pancreas;
RX PubMed=9211930; DOI=10.1074/jbc.272.28.17776;
RA McNew J.A., Soegaard M., Lampen N.M., Machida S., Ye R.R., Lacomis L.,
RA Tempst P., Rothman J.E., Soellner T.H.;
RT "Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi
RT transport.";
RL J. Biol. Chem. 272:17776-17783(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hepatoma;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-42; CYS-194 AND CYS-195, AND
RP PALMITOYLATION AT CYS-194.
RX PubMed=15479160; DOI=10.1042/BJ20041474;
RA Veit M.;
RT "The human SNARE protein Ykt6 mediates its own palmitoylation at C-
RT terminal cysteine residues.";
RL Biochem. J. 384:233-237(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14742712; DOI=10.1091/mbc.E03-08-0625;
RA Volchuk A., Ravazzola M., Perrelet A., Eng W.S., Di Liberto M.,
RA Varlamov O., Fukasawa M., Engel T., Sollner T.H., Rothman J.E.,
RA Orci L.;
RT "Countercurrent distribution of two distinct SNARE complexes mediating
RT transport within the Golgi stack.";
RL Mol. Biol. Cell 15:1506-1518(2004).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15215310; DOI=10.1091/mbc.E03-12-0876;
RA Tai G., Lu L., Wang T.L., Tang B.L., Goud B., Johannes L., Hong W.;
RT "Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in
RT transport from the early/recycling endosome to the trans-Golgi
RT network.";
RL Mol. Biol. Cell 15:4011-4022(2004).
RN [9]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-42; CYS-194 AND CYS-195,
RP ISOPRENYLATION AT CYS-195, AND PALMITOYLATION.
RX PubMed=15044687; DOI=10.1073/pnas.0401183101;
RA Fukasawa M., Varlamov O., Eng W.S., Soellner T.H., Rothman J.E.;
RT "Localization and activity of the SNARE Ykt6 determined by its
RT regulatory domain and palmitoylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4815-4820(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Vesicular soluble NSF attachment protein receptor (v-
CC SNARE) mediating vesicle docking and fusion to a specific acceptor
CC cellular compartment. Functions in endoplasmic reticulum to Golgi
CC transport; as part of a SNARE complex composed of GOSR1, GOSR2 and
CC STX5. Functions in early/recycling endosome to TGN transport; as
CC part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a
CC S-palmitoyl transferase activity.
CC -!- SUBUNIT: Identified in 2 different SNARE complexes; the first one
CC composed of GOSR1, GOSR2 and STX5 and the second one composed of
CC BET1L, GOSR1 and STX5 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasmic vesicle
CC membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus
CC membrane; Lipid-anchor; Cytoplasmic side. Note=Probably cycles
CC through vesicles between Golgi and endosomes.
CC -!- DOMAIN: The longin domain regulates palmitoylation and membrane
CC targeting.
CC -!- PTM: Palmitoylated; catalyzes its own palmitoylation.
CC Palmitoylation is required for Golgi targeting.
CC -!- PTM: Farnesylation is required for Golgi targeting.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC -!- SIMILARITY: Contains 1 longin domain.
CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
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DR EMBL; U95735; AAB81131.1; -; mRNA.
DR EMBL; BT007078; AAP35741.1; -; mRNA.
DR EMBL; CR456989; CAG33270.1; -; mRNA.
DR EMBL; CR542008; CAG46805.1; -; mRNA.
DR EMBL; AK223488; BAD97208.1; -; mRNA.
DR EMBL; BC007319; AAH07319.1; -; mRNA.
DR RefSeq; NP_006546.1; NM_006555.3.
DR UniGene; Hs.520794; -.
DR ProteinModelPortal; O15498; -.
DR SMR; O15498; 1-192.
DR IntAct; O15498; 1.
DR MINT; MINT-2999058; -.
DR STRING; 9606.ENSP00000223369; -.
DR PhosphoSite; O15498; -.
DR PaxDb; O15498; -.
DR PRIDE; O15498; -.
DR DNASU; 10652; -.
DR Ensembl; ENST00000223369; ENSP00000223369; ENSG00000106636.
DR GeneID; 10652; -.
DR KEGG; hsa:10652; -.
DR UCSC; uc003tkm.3; human.
DR CTD; 10652; -.
DR GeneCards; GC07P044207; -.
DR HGNC; HGNC:16959; YKT6.
DR HPA; HPA030817; -.
DR HPA; HPA030818; -.
DR MIM; 606209; gene.
DR neXtProt; NX_O15498; -.
DR PharmGKB; PA145007308; -.
DR eggNOG; COG5143; -.
DR HOGENOM; HOG000189970; -.
DR HOVERGEN; HBG088939; -.
DR InParanoid; O15498; -.
DR KO; K08516; -.
DR OMA; KQNSCCE; -.
DR PhylomeDB; O15498; -.
DR GeneWiki; YKT6; -.
DR GenomeRNAi; 10652; -.
DR NextBio; 40495; -.
DR PRO; PR:O15498; -.
DR ArrayExpress; O15498; -.
DR Bgee; O15498; -.
DR CleanEx; HS_YKT6; -.
DR Genevestigator; O15498; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
DR GO; GO:0005768; C:endosome; IDA:HGNC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HGNC.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:HGNC.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0031201; C:SNARE complex; ISS:HGNC.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:HGNC.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IDA:HGNC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:HGNC.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:HGNC.
DR GO; GO:0006903; P:vesicle targeting; IDA:HGNC.
DR Gene3D; 3.30.450.50; -; 1.
DR InterPro; IPR011012; Longin-like_dom.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR001388; Synaptobrevin.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS00417; SYNAPTOBREVIN; FALSE_NEG.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Lipoprotein; Membrane;
KW Methylation; Palmitate; Prenylation; Protein transport;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1 195 Synaptobrevin homolog YKT6.
FT /FTId=PRO_0000280709.
FT PROPEP 196 198 Removed in mature form (Probable).
FT /FTId=PRO_0000396661.
FT DOMAIN 8 126 Longin.
FT DOMAIN 138 198 v-SNARE coiled-coil homology.
FT MOD_RES 195 195 Cysteine methyl ester (Probable).
FT LIPID 194 194 S-palmitoyl cysteine.
FT LIPID 195 195 S-farnesyl cysteine.
FT MUTAGEN 42 42 F->E: Increases palmitoylation. Targeted
FT to Golgi membranes. Targeted to Golgi and
FT cytosol; when associated with S-194.
FT Targeted to cytosol; when associated with
FT S-195.
FT MUTAGEN 194 194 C->S: Decreases palmitoylation by 55%.
FT Prevents palmitoylation; when associated
FT with S-195. Targeted to Golgi and
FT cytosol; when associated with E-42.
FT MUTAGEN 195 195 C->S: Prevents farnesylation. Targeted to
FT cytosol; when associated with E-42.
FT Decreases palmitoylation by 13%. Prevents
FT palmitoylation; when associated with S-
FT 194.
FT CONFLICT 63 63 D -> N (in Ref. 3; CAG46805).
FT CONFLICT 138 138 P -> L (in Ref. 4; BAD97208).
FT CONFLICT 198 198 M -> I (in Ref. 3; CAG33270).
SQ SEQUENCE 198 AA; 22418 MW; 2AB0C12832D1B943 CRC64;
MKLYSLSVLY KGEAKVVLLK AAYDVSSFSF FQRSSVQEFM TFTSQLIVER SSKGTRASVK
EQDYLCHVYV RNDSLAGVVI ADNEYPSRVA FTLLEKVLDE FSKQVDRIDW PVGSPATIHY
PALDGHLSRY QNPREADPMT KVQAELDETK IILHNTMESL LERGEKLDDL VSKSEVLGTQ
SKAFYKTARK QNSCCAIM
//

MIM 606209
*RECORD*
*FIELD* NO
606209
*FIELD* TI
*606209 YKT6, S. CEREVISIAE, HOMOLOG OF; YKT6
*FIELD* TX

DESCRIPTION

For an explanation of the SNARE hypothesis, see 603215. YKT6 is a
read morev-SNARE involved in endoplasmic reticulum-Golgi transport.

CLONING

McNew et al. (1997) isolated S. cerevisiae Ykt6p as an interacting
partner of the cis Golgi target membrane-associated SNARE Sed5p. They
identified human YKT6 by comparison of the yeast sequence with an EST
database, and cloned the human cDNA by PCR from a pancreatic cDNA
library. Ykt6 and its homologs are highly conserved from yeast to human.
Human YKT6 protein shares 47% and 57% sequence identity with S.
cerevisiae and C. elegans homologs, respectively.

GENE FUNCTION

Ykt6 is an essential gene that codes for a novel vesicle-associated
SNARE functioning at the endoplasmic reticulum/Golgi transport step in
the yeast secretory pathway. McNew et al. (1997) demonstrated that
depletion of Ykt6p results in the accumulation of the p1 precursor of
the vacuolar enzyme carboxypeptidase Y and morphologic abnormalities
consistent with a defect in secretion. Membrane localization of Ykt6p is
essential for protein function and is normally mediated by
isoprenylation. However, replacement of the isoprenylation motif with a
bona fide transmembrane anchor results in a functional protein
confirming that membrane localization, but not isoprenylation per se, is
required for function. McNew et al. (1997) demonstrated that human YKT6
could complement the loss of Ykt6p.

Tochio et al. (2001) performed in vitro studies which revealed that the
N-terminal domain of Ykt6p plays an important biologic role in its
function, which includes influencing the kinetics and proper assembly of
SNARE complexes.

BIOCHEMICAL FEATURES

- Atomic Structure

By nuclear magnetic resonance (NMR) spectroscopy, Tochio et al. (2001)
reported the atomic structure of the N-terminal domain of Ykt6p. The
N-terminal structure of Ykt6p differed entirely from that of syntaxin
(see 186590) and resembled the overall fold of the actin regulatory
protein profilin (see 176610). Like some syntaxins, Ykt6p adopted a
folded-back conformation in which the Ykt6p N-terminus bound to its
C-terminal core domain.

*FIELD* RF
1. McNew, J. A.; Sogaard, M.; Lampen, N. M.; Machida, S.; Ye, R. R.;
Lacomis, L.; Tempst, P.; Rothman, J. E.; Sollner, T. H.: Ykt6p, a
prenylated SNARE essential for endoplasmic reticulum-Golgi transport. J.
Biol. Chem. 272: 17776-17783, 1997.

2. Tochio, H.; Tsui, M. M. K.; Banfield, D. K.; Zhang, M.: An autoinhibitory
mechanism for nonsyntaxin SNARE proteins revealed by the structure
of Ykt6p. Science 293: 698-702, 2001.

*FIELD* CD
Ada Hamosh: 8/20/2001

*FIELD* ED
alopez: 01/02/2007
alopez: 8/20/2001

RBCC Red Blood Cell Collection

Full text data of YKT6